5O8H
 
 | | Crystal structure of R. ruber ADH-A, mutant Y294F, W295A, F43H, H39Y | | 分子名称: | Alcohol dehydrogenase, GLYCEROL, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... | | 著者 | Dobritzsch, D, Maurer, D, Hamnevik, E, Reddy Enugala, T, Widersten, M. | | 登録日 | 2017-06-13 | | 公開日 | 2017-10-11 | | 最終更新日 | 2024-01-17 | | 実験手法 | X-RAY DIFFRACTION (1.96 Å) | | 主引用文献 | Relaxation of nonproductive binding and increased rate of coenzyme release in an alcohol dehydrogenase increases turnover with a nonpreferred alcohol enantiomer.
FEBS J., 284, 2017
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5O9F
 | | Crystal structure of R. ruber ADH-A, mutant Y294F, W295A, Y54F, F43S, H39Y | | 分子名称: | (2~{S})-2-methylpentanedioic acid, Alcohol dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... | | 著者 | Dobritzsch, D, Maurer, D, Hamnevik, E, Enugala, T.R, Widersten, M. | | 登録日 | 2017-06-19 | | 公開日 | 2017-10-11 | | 最終更新日 | 2024-01-17 | | 実験手法 | X-RAY DIFFRACTION (1.64 Å) | | 主引用文献 | Relaxation of nonproductive binding and increased rate of coenzyme release in an alcohol dehydrogenase increases turnover with a nonpreferred alcohol enantiomer.
FEBS J., 284, 2017
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5O9D
 | | Crystal structure of R. ruber ADH-A, mutant Y294F, W295A, Y54F, F43H, H39Y | | 分子名称: | (2~{S})-2-methylpentanedioic acid, Alcohol dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... | | 著者 | Dobritzsch, D, Maurer, D, Hamnevik, E, Enugala, T.R, Widersten, M. | | 登録日 | 2017-06-19 | | 公開日 | 2017-10-11 | | 最終更新日 | 2024-01-17 | | 実験手法 | X-RAY DIFFRACTION (1.79 Å) | | 主引用文献 | Relaxation of nonproductive binding and increased rate of coenzyme release in an alcohol dehydrogenase increases turnover with a nonpreferred alcohol enantiomer.
FEBS J., 284, 2017
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5O8Q
 | | Crystal structure of R. ruber ADH-A, mutant Y294F, W295A | | 分子名称: | Alcohol dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ZINC ION | | 著者 | Dobritzsch, D, Maurer, D, Hamnevik, E, Enugala, T.R, Widersten, M. | | 登録日 | 2017-06-14 | | 公開日 | 2017-10-11 | | 最終更新日 | 2024-01-17 | | 実験手法 | X-RAY DIFFRACTION (2.22 Å) | | 主引用文献 | Relaxation of nonproductive binding and increased rate of coenzyme release in an alcohol dehydrogenase increases turnover with a nonpreferred alcohol enantiomer.
FEBS J., 284, 2017
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